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Article

Inhibitory characteristics and oxidant resistance of site specific variants of recombinant human antileukoproteinase (ALP).

Biomedica biochimica acta - 1 Jan 1991

Heinzel-Wieland R, Steffens G J, Flohé L

Abstract excerpt

Tandem gene plasmids were constructed and used to express inactive proteins equivalent to human antileukoproteinase (ALP) and the variants [Leu73]-ALP and [Leu73, 82, 94, 96]-ALP in E. coli K12. After extraction, refolding, and purification, highly pure and active inhibitors were obtained in good yields. Inhibitory constants for human leukocyte elastase and cathepsin G were found to be similar. The variants in...

Topics

Escherichia coli
Genetic Variation
Humans
Kinetics
Mutagenesis, Site-Directed
Oxidation-Reduction
Plasmids
Proteinase Inhibitory Proteins, Secretory
Proteins
Recombinant Proteins
Serine Proteinase Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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PMID: 1801742

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1801742-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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